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7QJR

Crystal structure of cutinase 1 from Thermobifida fusca DSM44342 (703)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0016787molecular_functionhydrolase activity
A0042597cellular_componentperiplasmic space
A0050525molecular_functioncutinase activity
A0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. LAVMGHSMGG
ChainResidueDetails
ALEU125-GLY134

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"24728714","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CG2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"A0A0K8P6T7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"A0A0K8P6T7","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"24728714","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"A0A0K8P6T7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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